Details for: MBD2
Associated with
Other Information
Genular Protein ID: 87634078
Symbol: MBD2_HUMAN
Name: Demethylase
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 9774669
Title: Identification and characterization of a family of mammalian methyl-CpG binding proteins.
PubMed ID: 9774669
PubMed ID: 10441743
Title: Genomic structure and chromosomal mapping of the murine and human mbd1, mbd2, mbd3, and mbd4 genes.
PubMed ID: 10441743
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 10050851
Title: A mammalian protein with specific demethylase activity for mCpG DNA.
PubMed ID: 10050851
DOI: 10.1038/17533
PubMed ID: 10471499
Title: MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex.
PubMed ID: 10471499
DOI: 10.1038/12659
PubMed ID: 10947852
Title: MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase.
PubMed ID: 10947852
PubMed ID: 10950960
Title: The minimal repression domain of MBD2b overlaps with the methyl-CpG-binding domain and binds directly to Sin3A.
PubMed ID: 10950960
PubMed ID: 11102443
Title: Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1.
PubMed ID: 11102443
PubMed ID: 11553631
Title: Involvement of a novel zinc finger protein, MIZF, in transcriptional repression by interacting with a methyl-CpG-binding protein, MBD2.
PubMed ID: 11553631
PubMed ID: 12183469
Title: Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3.
PubMed ID: 12183469
PubMed ID: 12588985
Title: MBDin, a novel MBD2-interacting protein, relieves MBD2 repression potential and reactivates transcription from methylated promoters.
PubMed ID: 12588985
PubMed ID: 12665568
Title: Antithetic effects of MBD2a on gene regulation.
PubMed ID: 12665568
PubMed ID: 15701600
Title: MBD3L2 interacts with MBD3 and components of the NuRD complex and can oppose MBD2-MeCP1-mediated methylation silencing.
PubMed ID: 15701600
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 16428440
Title: MBD2/NuRD and MBD3/NuRD, two distinct complexes with different biochemical and functional properties.
PubMed ID: 16428440
PubMed ID: 16415179
Title: p66alpha and p66beta of the Mi-2/NuRD complex mediate MBD2 and histone interaction.
PubMed ID: 16415179
DOI: 10.1093/nar/gkj437
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19729656
Title: Regulation of histone acetylation in the nucleus by sphingosine-1-phosphate.
PubMed ID: 19729656
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 20523938
Title: CDK2AP1/DOC-1 is a bona fide subunit of the Mi-2/NuRD complex.
PubMed ID: 20523938
DOI: 10.1039/c004108d
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24307175
Title: Probing the dynamic distribution of bound states for methylcytosine-binding domains on DNA.
PubMed ID: 24307175
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 27732854
Title: ZMYND8 Co-localizes with NuRD on Target Genes and Regulates Poly(ADP-Ribose)-Dependent Recruitment of GATAD2A/NuRD to Sites of DNA Damage.
PubMed ID: 27732854
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 28977666
Title: CHD3 and CHD4 form distinct NuRD complexes with different yet overlapping functionality.
PubMed ID: 28977666
DOI: 10.1093/nar/gkx711
PubMed ID: 33283408
Title: Cross-linking mass spectrometry reveals the structural topology of peripheral NuRD subunits relative to the core complex.
PubMed ID: 33283408
DOI: 10.1111/febs.15650
PubMed ID: 21490301
Title: p66Alpha-MBD2 coiled-coil interaction and recruitment of Mi-2 are critical for globin gene silencing by the MBD2-NuRD complex.
PubMed ID: 21490301
Sequence Information:
- Length: 411
- Mass: 43255
- Checksum: FC4E5E0CF9BA0FFA
- Sequence:
MRAHPGGGRC CPEQEEGESA AGGSGAGGDS AIEQGGQGSA LAPSPVSGVR REGARGGGRG RGRWKQAGRG GGVCGRGRGR GRGRGRGRGR GRGRGRPPSG GSGLGGDGGG CGGGGSGGGG APRREPVPFP SGSAGPGPRG PRATESGKRM DCPALPPGWK KEEVIRKSGL SAGKSDVYYF SPSGKKFRSK PQLARYLGNT VDLSSFDFRT GKMMPSKLQK NKQRLRNDPL NQNKGKPDLN TTLPIRQTAS IFKQPVTKVT NHPSNKVKSD PQRMNEQPRQ LFWEKRLQGL SASDVTEQII KTMELPKGLQ GVGPGSNDET LLSAVASALH TSSAPITGQV SAAVEKNPAV WLNTSQPLCK AFIVTDEDIR KQEERVQQVR KKLEEALMAD ILSRAADTEE MDIEMDSGDE A
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.